The structure of (3R)-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Pseudomonas aeruginosa.

@article{Kimber2004TheSO,
  title={The structure of (3R)-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Pseudomonas aeruginosa.},
  author={Matthew S Kimber and Fernando Tadeu Bueno Martin and Yingjie Lu and Simon Houston and Masoud Vedadi and Akil Dharamsi and Klaus M. Fiebig and Molly B. Schmid and Charles O Rock},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 50},
  pages={52593-602}
}
Type II fatty acid biosynthesis systems are essential for membrane formation in bacteria, making the constituent proteins of this pathway attractive targets for antibacterial drug discovery. The third step in the elongation cycle of the type II fatty acid biosynthesis is catalyzed by beta-hydroxyacyl-(acyl carrier protein) (ACP) dehydratase. There are two isoforms. FabZ, which catalyzes the dehydration of (3R)-hydroxyacyl-ACP to trans-2-acyl-ACP, is a universally expressed component of the… CONTINUE READING

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